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Related Concept Videos

Ribosomes01:27

Ribosomes

9.8K
Ribosomes translate genetic information encoded by messenger RNA (mRNA) into proteins. Both prokaryotic and eukaryotic cells have ribosomes. Cells that synthesize large quantities of protein—such as secretory cells in the human pancreas—can contain millions of ribosomes.
Ribosome Structure and Assembly
Ribosomes are composed of ribosomal RNA (rRNA) and proteins. In eukaryotes, rRNA is transcribed from genes in the nucleolus—a part of the nucleus that specializes in ribosome...
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Ribosomes01:27

Ribosomes

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Ribosomes translate genetic information encoded by messenger RNA (mRNA) into proteins. Both prokaryotic and eukaryotic cells have ribosomes. Cells that synthesize large quantities of protein—such as secretory cells in the human pancreas—can contain millions of ribosomes.
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Ribosomal RNA Synthesis02:53

Ribosomal RNA Synthesis

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Ribosome synthesis is a highly complex and coordinated process involving more than 200 assembly factors. The synthesis and processing of ribosomal components occurs not only in the nucleolus but also in the nucleoplasm and the cytoplasm of eukaryotic cells.
Ribosome biogenesis begins with the synthesis of 5S and 45S pre-rRNAs by distinct RNA polymerases. The primary transcripts are extensively processed and modified before they are bound and folded by ribosomal proteins and assembly factors,...
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Ribosomal RNA Synthesis02:53

Ribosomal RNA Synthesis

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Termination of Translation01:44

Termination of Translation

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The large ribosomal subunit has several important structures essential to translation. These include the peptidyl transferase center (PTC) - which is the site where the peptide bond is formed - and a large, internal, water-filled tube through which the nascent polypeptide moves. This latter structure is called the Peptide Exit Tunnel, and it begins at the PTC and spans the body of the large ribosomal subunit. During translation, as the nascent polypeptide chain is synthesized, it passes through...
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Improving Translational Accuracy02:07

Improving Translational Accuracy

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Base complementarity between the three base pairs of mRNA codon and the tRNA anticodon is not a failsafe mechanism. Inaccuracies can range from a single mismatch to no correct base pairing at all. The free energy difference between the correct and nearly correct base pairs can be as small as 3 kcal/ mol. With complementarity being the only proofreading step, the estimated error frequency would be one wrong amino acid in every 100 amino acids incorporated. However, error frequencies observed in...
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Updated: Dec 27, 2025

Single Molecule Fluorescence Energy Transfer Study of Ribosome Protein Synthesis
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Ribosome Dimerization Protects the Small Subunit.

Heather A Feaga1, Mykhailo Kopylov2, Jenny Kim Kim3

  • 1Department of Microbiology and Immunology, College of Physicians and Surgeons, Columbia University, New York, New York, USA.

Journal of Bacteriology
|March 4, 2020
PubMed
Summary
This summary is machine-generated.

Hibernation-promoting factor (HPF) protects bacteria during nutrient scarcity by preventing the loss of essential ribosomal proteins S2 and S3. This ribosome dimerization mechanism ensures bacterial survival and rapid regrowth when conditions improve.

Keywords:
stationary phasetranslation

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Area of Science:

  • Bacteriology
  • Molecular Biology
  • Structural Biology

Background:

  • Bacteria enter a quiescent state when nutrients are scarce.
  • Preserving ribosomes is crucial for bacterial survival during dormancy.
  • Ribosome dimerization, mediated by hibernation-promoting factor (HPF), is common in quiescent bacteria.

Purpose of the Study:

  • To elucidate the protective mechanism of HPF during bacterial quiescence.
  • To investigate the role of HPF in preserving essential ribosomal proteins.
  • To understand how HPF-mediated ribosome dimerization aids bacterial survival.

Main Methods:

  • Analysis of bacterial strains lacking or with mutant HPF.
  • Biochemical isolation of ribosomes.
  • Single-particle cryo-electron microscopy (cryo-EM) to characterize ribosome structure.

Main Results:

  • Strains lacking functional HPF showed depletion of ribosomal proteins S2 and S3.
  • S2 and S3 are located at the ribosome dimer interface.
  • Cryo-EM revealed missing S2, S3, or both in ribosomes lacking HPF's dimerization function.

Conclusions:

  • HPF's dimerization activity protects labile ribosomal proteins S2 and S3.
  • This protection mechanism is vital for bacterial survival during nutrient limitation.
  • HPF-mediated ribosome stabilization explains observed defects in HPF-deficient bacteria.